3j4k

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3j4k]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J4K FirstGlance]. <br>
<table><tr><td colspan='2'>[[3j4k]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J4K FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j4k OCA], [https://pdbe.org/3j4k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j4k RCSB], [https://www.ebi.ac.uk/pdbsum/3j4k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j4k ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j4k OCA], [https://pdbe.org/3j4k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j4k RCSB], [https://www.ebi.ac.uk/pdbsum/3j4k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j4k ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
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[https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Tropomyosin (Tm) is a key factor in the molecular mechanisms that regulate the binding of myosin motors to actin filaments (F-Actins) in most eukaryotic cells. This regulation is achieved by the azimuthal repositioning of Tm along the actin (Ac):Tm:troponin (Tn) thin filament to block or expose myosin binding sites on Ac. In striated muscle, including involuntary cardiac muscle, Tm regulates muscle contraction by coupling Ca2+ binding to Tn with myosin binding to the thin filament. In smooth muscle, the switch is the posttranslational modification of the myosin. Depending on the activation state of Tn and the binding state of myosin, Tm can occupy the blocked, closed, or open position on Ac. Using native cryogenic 3DEM (three-dimensional electron microscopy), we have directly resolved and visualized cardiac and gizzard muscle Tm on filamentous Ac in the position that corresponds to the closed state. From the 8-A-resolution structure of the reconstituted Ac:Tm filament formed with gizzard-derived Tm, we discuss two possible mechanisms for the transition from closed to open state and describe the role Tm plays in blocking myosin tight binding in the closed-state position.
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Cryo-EM Structures of the Actin:Tropomyosin Filament Reveal the Mechanism for the Transition from C- to M-State.,Sousa DR, Stagg SM, Stroupe ME J Mol Biol. 2013 Sep 8. pii: S0022-2836(13)00540-8. doi:, 10.1016/j.jmb.2013.08.020. PMID:24021812<ref>PMID:24021812</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3j4k" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Actin 3D structures|Actin 3D structures]]
*[[Actin 3D structures|Actin 3D structures]]
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*[[Tropomyosin|Tropomyosin]]
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*[[Tropomyosin 3D structures|Tropomyosin 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</SX>
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Sousa, D R]]
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[[Category: Sousa DR]]
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[[Category: Stagg, S M]]
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[[Category: Stagg SM]]
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[[Category: Stroupe, M E]]
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[[Category: Stroupe ME]]
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[[Category: Actin]]
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[[Category: Coiled-coil c-state]]
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[[Category: Structural protein]]
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[[Category: Tropomyosin]]
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Current revision

Cryo-EM structures of the actin:tropomyosin filament reveal the mechanism for the transition from C- to M-state

3j4k, resolution 8.00Å

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